Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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cysISulfite reductase (hemoprotein beta-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (Probable); Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (571 aa)    
Predicted Functional Partners:
cysH
(phospho)adenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite.
 
 0.999
cysJ
Sulfite reductase (flavoprotein alpha-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable).
 0.999
cysC
Adenylylsulfate kinase; Catalyzes the synthesis of activated sulfate; Belongs to the APS kinase family.
  
  
 0.992
yitB
Putative phospho-adenylylsulfate sulfotransferase; Reduction of activated sulfate into sulfite; Belongs to the PAPS reductase family. CysH subfamily.
 
 0.991
cysK
Cysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
  
 
 0.985
cypD
Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS).
 
 
 0.963
cypB
Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.
 
 
 0.960
mccB
Cystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide.
  
 
 0.957
ytkP
Putative cysteine synthase-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
 
 0.948
metI
Cystathionine gamma-synthase and O-acetylhomoserine thiolyase; Catalyzes the formation of L-cystathionine from O-acetyl-L- homoserine and L-cysteine. Cannot use O-succinyl-L-homoserine as substrate. Also exhibits O-acetylhomoserine thiolyase activity, catalyzing the synthesis of L-homocysteine from O-acetyl-L-homoserine and sulfide.
  
 
 0.932
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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